EMD-21398
Porcine epidemic diarrhea virus (PEDV) spike protein bound to negative control polyclonal Fab
EMD-21398
Single-particle15.0 Å
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Map released: 26/02/2020
Last modified: 14/04/2021
Sample Organism:
Porcine epidemic diarrhea virus
Sample: Porcine epidemic diarrhea virus spike protein bound to negative control polyclonal Fab.
Deposition Authors: Kirchdoerfer RN, Martini O, Sewall LM, Bangaru S, Ward AB
Sample: Porcine epidemic diarrhea virus spike protein bound to negative control polyclonal Fab.
Deposition Authors: Kirchdoerfer RN, Martini O, Sewall LM, Bangaru S, Ward AB
Structure and immune recognition of the porcine epidemic diarrhea virus spike protein.
Kirchdoerfer RN,
Bhandari M
,
Martini O,
Sewall LM
,
Bangaru S
,
Yoon KJ,
Ward AB
(2021) Structure , 29 , 385 - 392.e5
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(2021) Structure , 29 , 385 - 392.e5
Abstract:
Porcine epidemic diarrhea virus (PEDV) is an alphacoronavirus responsible for significant morbidity and mortality in pigs. A key determinant of viral tropism and entry, the PEDV spike protein is a key target for the host antibody response and a good candidate for a protein-based vaccine immunogen. We used electron microscopy to evaluate the PEDV spike structure, as well as pig polyclonal antibody responses to viral infection. The structure of the PEDV spike reveals a configuration similar to that of HuCoV-NL63. Several PEDV protein-protein interfaces are mediated by non-protein components, including a glycan at Asn264 and two bound palmitoleic acid molecules. The polyclonal antibody response to PEDV infection shows a dominance of epitopes in the S1 region. This structural and immune characterization provides insights into coronavirus spike stability determinants and explores the immune landscape of viral spike proteins.
Porcine epidemic diarrhea virus (PEDV) is an alphacoronavirus responsible for significant morbidity and mortality in pigs. A key determinant of viral tropism and entry, the PEDV spike protein is a key target for the host antibody response and a good candidate for a protein-based vaccine immunogen. We used electron microscopy to evaluate the PEDV spike structure, as well as pig polyclonal antibody responses to viral infection. The structure of the PEDV spike reveals a configuration similar to that of HuCoV-NL63. Several PEDV protein-protein interfaces are mediated by non-protein components, including a glycan at Asn264 and two bound palmitoleic acid molecules. The polyclonal antibody response to PEDV infection shows a dominance of epitopes in the S1 region. This structural and immune characterization provides insights into coronavirus spike stability determinants and explores the immune landscape of viral spike proteins.